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925225

Sigma-Aldrich

KB02yne

Synonym(s):

2-Chloro-1-(6-(hex-5-yn-1-yloxy)-3,4-dihydroquinolin-1(2H)-yl)ethan-1-one, Functionalized scout fragment

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About This Item

Empirical Formula (Hill Notation):
C17H20ClNO2
CAS Number:
2376152-06-4
Molecular Weight:
305.80
UNSPSC Code:
12352101
NACRES:
NA.22

form

powder or crystals (or Solid or Liquid)

Quality Level

100

reaction suitability

reagent type: chemical modification reagent
reaction type: click chemistry

storage temp.

2-8°C

Related Categories

Application

KB02yne is a cysteine-reactive small-molecule fragment for chemoproteomic and ligandability studies for both traditionally druggable proteins as well as ″undruggable,″ or difficult-to-target, proteins. This fragment electrophile is the functionalized version of KB02 (912131).

Related useful products may include:
  • Cysteine-reactive fragments: KB02 (912131), KB03 (912654), KB05 (911798), sulfoxide (925136), CoLDR probe (923818)
  • Functionalized scout fragments: KB02-COOH (925047), KB05yne (925144)
  • Electrophilc degraders featuring scout fragments: KB02-SLF (914738), KB03-SLF (914975), KB05-SLF (913715), Biotin-SLF (914223)
  • Cysteine-reactive probes for chemoproteomics: IA alkyne (924237), IA 5-TAMRA (925020), desthiobiotin iodoacetamide (923826), or biotin iodoacetamide (B2059)

Technology spotlight: Proteomic Ligandability Assessment

Other Notes

Functionalized Scout Fragments for Site-Specific Covalent Ligand Discovery and Optimization

The Proteome-Wide Potential for Reversible Covalency at Cysteine

Electrophilic PROTACs that degrade nuclear proteins by engaging DCAF16

related product

Product No.
Description
Pricing

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Certificates of Analysis (COA)

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Kristine Senkane et al.
Angewandte Chemie (International ed. in English), 58(33), 11385-11389 (2019-06-22)
Reversible covalency, achieved with, for instance, highly electron-deficient olefins, offers a compelling strategy to design chemical probes and drugs that benefit from the sustained target engagement afforded by irreversible compounds, while avoiding permanent protein modification. Reversible covalency has mainly been

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